IABN_GEOSE
ID IABN_GEOSE Reviewed; 315 AA.
AC B3EYM8;
DT 01-MAY-2013, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 45.
DE RecName: Full=Intracellular endo-alpha-(1->5)-L-arabinanase;
DE Short=ABN;
DE EC=3.2.1.99;
DE AltName: Full=Endo-1,5-alpha-L-arabinanase;
GN Name=abnB;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=8031084; DOI=10.1128/aem.60.6.1889-1896.1994;
RA Gat O., Lapidot A., Alchanati I., Regueros C., Shoham Y.;
RT "Cloning and DNA sequence of the gene coding for Bacillus
RT stearothermophilus T-6 xylanase.";
RL Appl. Environ. Microbiol. 60:1889-1896(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=10368143; DOI=10.1128/jb.181.12.3695-3704.1999;
RA Shulami S., Gat O., Sonenshein A.L., Shoham Y.;
RT "The glucuronic acid utilization gene cluster from Bacillus
RT stearothermophilus T-6.";
RL J. Bacteriol. 181:3695-3704(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=11358519; DOI=10.1046/j.1432-1327.2001.02193.x;
RA Zaide G., Shallom D., Shulami S., Zolotnitsky G., Golan G., Baasov T.,
RA Shoham G., Shoham Y.;
RT "Biochemical characterization and identification of catalytic residues in
RT alpha-glucuronidase from Bacillus stearothermophilus T-6.";
RL Eur. J. Biochem. 268:3006-3016(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=11322943; DOI=10.1016/s0014-5793(01)02360-2;
RA Bravman T., Zolotnitsky G., Shulami S., Belakhov V., Solomon D., Baasov T.,
RA Shoham G., Shoham Y.;
RT "Stereochemistry of family 52 glycosyl hydrolases: a beta-xylosidase from
RT Bacillus stearothermophilus T-6 is a retaining enzyme.";
RL FEBS Lett. 495:39-43(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RX PubMed=17142383; DOI=10.1128/aem.02367-06;
RA Shulami S., Zaide G., Zolotnitsky G., Langut Y., Feld G., Sonenshein A.L.,
RA Shoham Y.;
RT "A two-component system regulates the expression of an ABC transporter for
RT xylo-oligosaccharides in Geobacillus stearothermophilus.";
RL Appl. Environ. Microbiol. 73:874-884(2007).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=T-6;
RA Shoham Y., Shulami S., Ben-David A., Langut Y.;
RT "Hemicellulose utilization cluster in Geobacillus stearothermophilus strain
RT T-6.";
RL Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INDUCTION.
RX PubMed=21460081; DOI=10.1128/jb.00222-11;
RA Shulami S., Raz-Pasteur A., Tabachnikov O., Gilead-Gropper S., Shner I.,
RA Shoham Y.;
RT "The L-Arabinan utilization system of Geobacillus stearothermophilus.";
RL J. Bacteriol. 193:2838-2850(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (1.06 ANGSTROMS) OF 2-315 OF MUTANTS ALA-27; ALA-201
RP AND ALA-1747 IN COMPLEX WITH ALPHA-L-ARABINOFURANOSE AND CALCIUM ION,
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, COFACTOR, SUBCELLULAR LOCATION,
RP SUBSTRATE SPECIFICITY, AND SUBUNIT.
RX PubMed=19505290; DOI=10.1042/bj20090180;
RA Alhassid A., Ben-David A., Tabachnikov O., Libster D., Naveh E.,
RA Zolotnitsky G., Shoham Y., Shoham G.;
RT "Crystal structure of an inverting GH 43 1,5-alpha-L-arabinanase from
RT Geobacillus stearothermophilus complexed with its substrate.";
RL Biochem. J. 422:73-82(2009).
CC -!- FUNCTION: Involved in the degradation of arabinan and is a key enzyme
CC in the complete degradation of the plant cell wall. Catalyzes the
CC internal cleavage of alpha-(1->5)-L-arabinofuranosyl residues of
CC debranched arabinan, linear arabinan and short arabino-oligosaccharides
CC (degree of polymerization from 2 to 8). It exhibits marginal activity
CC toward sugar beet arabinan. {ECO:0000269|PubMed:19505290}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->5)-alpha-arabinofuranosidic linkages in
CC (1->5)-arabinans.; EC=3.2.1.99;
CC Evidence={ECO:0000269|PubMed:19505290};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305};
CC -!- PATHWAY: Glycan metabolism; L-arabinan degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19505290}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:19505290}.
CC -!- INDUCTION: Transcription is repressed by glucose and by the binding of
CC AraR to the operon promoter. L-arabinose acts as an inducer by
CC inhibiting the binding of AraR to the DNA, thus allowing expression of
CC the gene. {ECO:0000269|PubMed:21460081}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 43 family. {ECO:0000305}.
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DR EMBL; DQ868502; ACE73676.1; -; Genomic_DNA.
DR PDB; 3CU9; X-ray; 1.06 A; A=2-315.
DR PDB; 3D5Y; X-ray; 1.22 A; A=2-315.
DR PDB; 3D5Z; X-ray; 1.90 A; A=2-315.
DR PDB; 3D60; X-ray; 1.90 A; A=2-315.
DR PDB; 3D61; X-ray; 1.95 A; A=2-315.
DR PDB; 6F1G; X-ray; 1.67 A; A=1-315.
DR PDBsum; 3CU9; -.
DR PDBsum; 3D5Y; -.
DR PDBsum; 3D5Z; -.
DR PDBsum; 3D60; -.
DR PDBsum; 3D61; -.
DR PDBsum; 6F1G; -.
DR AlphaFoldDB; B3EYM8; -.
DR SMR; B3EYM8; -.
DR CAZy; GH43; Glycoside Hydrolase Family 43.
DR BRENDA; 3.2.1.99; 623.
DR UniPathway; UPA00667; -.
DR EvolutionaryTrace; B3EYM8; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0046558; F:arabinan endo-1,5-alpha-L-arabinosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0031222; P:arabinan catabolic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 2.115.10.20; -; 1.
DR InterPro; IPR006710; Glyco_hydro_43.
DR InterPro; IPR016840; Glyco_hydro_43_endo_a_Ara-ase.
DR InterPro; IPR023296; Glyco_hydro_beta-prop_sf.
DR Pfam; PF04616; Glyco_hydro_43; 1.
DR PIRSF; PIRSF026534; Endo_alpha-L-arabinosidase; 1.
DR SUPFAM; SSF75005; SSF75005; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Cytoplasm; Glycosidase;
KW Hydrolase; Metal-binding.
FT CHAIN 1..315
FT /note="Intracellular endo-alpha-(1->5)-L-arabinanase"
FT /id="PRO_0000422129"
FT ACT_SITE 27
FT /note="Proton acceptor"
FT /evidence="ECO:0000305|PubMed:19505290"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000305|PubMed:19505290"
FT BINDING 27
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19505290"
FT BINDING 105
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19505290"
FT BINDING 144..147
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19505290"
FT BINDING 164..166
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:19505290"
FT BINDING 271
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255"
FT SITE 147
FT /note="Important for catalytic activity, responsible for
FT pKa modulation of the active site Glu and correct
FT orientation of both the proton donor and substrate"
FT /evidence="ECO:0000305|PubMed:19505290"
FT SITE 271
FT /note="Important for substrate recognition"
FT /evidence="ECO:0000250"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 29..33
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 36..44
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 46..63
FT /evidence="ECO:0007829|PDB:3CU9"
FT HELIX 71..74
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 82..91
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 94..101
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 129..137
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 141..143
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 158..162
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:3CU9"
FT TURN 176..178
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:6F1G"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 194..197
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 200..208
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 211..219
FT /evidence="ECO:0007829|PDB:3CU9"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 230..238
FT /evidence="ECO:0007829|PDB:3CU9"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 257..260
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 264..277
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 280..289
FT /evidence="ECO:0007829|PDB:3CU9"
FT TURN 290..294
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 296..305
FT /evidence="ECO:0007829|PDB:3CU9"
FT STRAND 311..313
FT /evidence="ECO:0007829|PDB:3CU9"
SQ SEQUENCE 315 AA; 35763 MW; 86861395D823A044 CRC64;
MVHFHPFGNV NFYEMDWSLK GDLWAHDPVI AKEGSRWYVF HTGSGIQIKT SEDGVHWENM
GWVFPSLPDW YKQYVPEKDE DHLWAPDICF YNGIYYLYYS VSTFGKNTSV IGLATNQTLD
PRDPDYEWKD MGPVIHSTAS DNYNAIDPNV VFDQEGQPWL SFGSFWSGIQ LIQLDTETMK
PAAQAELLTI ASRGEEPNAI EAPFIVCRNG YYYLFVSFDF CCRGIESTYK IAVGRSKDIT
GPYVDKNGVS MMQGGGTILD EGNDRWIGPG HCAVYFSGVS AILVNHAYDA LKNGEPTLQI
RPLYWDDEGW PYLSV
